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  The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3 ' end.

Melero, R., Buchwald, G., Castano, R., Raabe, M., Gil, D., Lazaro, M., et al. (2012). The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3 ' end. Nature Structural and Molecular Biology, 19(5), 498-505. doi:10.1038/nsmb.2287.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000F-9FD1-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-1DEC-8
Genre: Journal Article

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 Creators:
Melero, R., Author
Buchwald, G., Author
Castano, R., Author
Raabe, M.1, Author              
Gil, D., Author
Lazaro, M., Author
Urlaub, H.1, Author              
Conti, E., Author
Llorca, O., Author
Affiliations:
1Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              

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 Abstract: Nonsense-mediated mRNA decay (NMD) is a eukaryotic surveillance pathway that degrades aberrant mRNAs containing premature termination codons (PTCs). NMD is triggered upon the assembly of the UPF surveillance complex near a PTC. In humans, UPF assembly is prompted by the exon junction complex (EJC). We investigated the molecular architecture of the human UPF complex bound to the EJC by cryo-EM and using positional restraints from additional EM, MS and biochemical interaction data. The heptameric assembly is built around UPF2, a scaffold protein with a ring structure that closes around the CH domain of UPF1, keeping the helicase region in an accessible and unwinding-competent state. UPF2 also positions UPF3 to interact with the EJC. The geometry is such that this transient complex poises UPF1 to elicit helicase activity toward the 3 ′ end of the mRNP.

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Language(s): eng - English
 Dates: 2012-04-222012-05
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/nsmb.2287
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Title: Nature Structural and Molecular Biology
Source Genre: Journal
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Pages: - Volume / Issue: 19 (5) Sequence Number: - Start / End Page: 498 - 505 Identifier: -